Vibrio cholerae Thiol Peroxidase-Glutaredoxin Fusion Is a 2-Cys TSA/AhpC Subfamily Acting as a Lipid Hydroperoxide Reductase

Cha, Mee‐Kyung; Hong, Seung–Keun; Lee, Dong-Suk; Kim, Il-Han

doi:10.1074/jbc.m312657200

Cited by 24 publications

(21 citation statements)

References 32 publications

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“…5 to 7). Different species of peroxiredoxins have been identified in bacteria, including the fusion protein of thiol peroxidase and glutaredoxin in V. cholerae (35). Functions of different AhpC species have been reported in a few studies.…”

Section: Discussionmentioning

confidence: 99%

Roles of Alkyl Hydroperoxide Reductase Subunit C (AhpC) in Viable but Nonculturable Vibrio parahaemolyticus

Wang

Chung

et al. 2013

Appl Environ Microbiol

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Alkyl hydroperoxide reductase subunit C (AhpC) is the catalytic subunit responsible for the detoxification of reactive oxygen species that form in bacterial cells or are derived from the host; thus, AhpC facilitates the survival of pathogenic bacteria under environmental stresses or during infection. This study investigates the role of AhpC in the induction and maintenance of a viable but nonculturable (VBNC) state in Vibrio parahaemolyticus. In this investigation, ahpC1 (VPA1683) and ahpC2 (VP0580) were identified in chromosomes II and I of this pathogen, respectively. Mutants with deletions of these two ahpC genes and their complementary strains were constructed from the parent strain KX-V231. The growth of these strains was monitored on tryptic soy agar-3% NaCl in the presence of the extrinsic peroxides H 2 O 2 and tert-butyl hydroperoxide (t-BOOH) at different incubation temperatures. The results revealed that both ahpC genes were protective against t-BOOH, while ahpC1 was protective against H 2 O 2 . The protective function of ahpC2 at 4°C was higher than that of ahpC1. The times required to induce the VBNC state (4.7 weeks) at 4°C in a modified Morita mineral salt solution with 0.5% NaCl and then to maintain the VBNC state (4.7 weeks) in an ahpC2 mutant and an ahpC1 ahpC2 double mutant were significantly shorter than those for the parent strain (for induction, 6.2 weeks; for maintenance, 7.8 weeks) and the ahpC1 mutant (for induction, 6.0 weeks; for maintenance, 8.0 weeks) (P < 0.03). Complementation with an ahpC2 gene reversed the effects of the ahpC2 mutation in shortening the times for induction and maintenance of the VBNC state. This investigation identified the different functions of the two ahpC genes and confirmed the particular role of ahpC2 in the VBNC state of V. parahaemolyticus.

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Section: Discussionmentioning

confidence: 99%

Roles of Alkyl Hydroperoxide Reductase Subunit C (AhpC) in Viable but Nonculturable Vibrio parahaemolyticus

Wang

Chung

et al. 2013

Appl Environ Microbiol

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“…Interestingly, some bacteria contain fusion proteins composed of a type II PRX followed by a GRX module. These proteins can use GSH to reduce a wide range of peroxide substrates (Pauwels et al 2003;Rouhier and Jacquot 2003;Cha et al 2004). Moreover, artificial hybrid proteins between poplar type II peroxiredoxin and glutaredoxin or thioredoxin h were recently engineered and shown to be functional, indicating that the two modules can function together .…”

Section: The Peroxiredoxin Familymentioning

confidence: 99%

The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

et al. 2008

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Thiol/selenol peroxidases are ubiquitous nonheme peroxidases. They are divided into two major subfamilies: peroxiredoxins (PRXs) and glutathione peroxidases (GPXs). PRXs are present in diverse subcellular compartments and divided into four types: 2-cys PRX, 1-cys PRX, PRX-Q , and type II PRX (PRXII). In mammals, most GPXs are selenoenzymes containing a highly reactive selenocysteine in their active site while yeast and land plants are devoid of selenoproteins but contain nonselenium GPXs. The presence of a chloroplastic 2-cys PRX, a nonselenium GPX, and two selenium-dependent GPXs has been reported in the unicellular green alga Chlamydomonas reinhardtii. The availability of the Chlamydomonas genome sequence offers the opportunity to complete our knowledge on thiol/selenol peroxidases in this organism. In this article, Chlamydomonas PRX and GPX families are presented and compared to their counterparts in Arabidopsis, human, yeast, and Synechocystis sp. A summary of the current knowledge on each family of peroxidases, especially in photosynthetic organisms, phylogenetic analyses, and investigations of the putative subcellular localization of each protein and its relative expression level, on the basis of EST data, are presented. We show that Chlamydomonas PRX and GPX families share some similarities with other photosynthetic organisms but also with human cells. The data are discussed in view of recent results suggesting that these enzymes are important scavengers of reactive oxygen species (ROS) and reactive nitrogen species (RNS) but also play a role in ROS signaling. L IFE in an oxygen-rich environment has to deal with the danger of oxidative stress. During normal cell metabolism, reactive oxygen species (ROS) and reactive nitrogen species (RNS) are constantly produced, essentially by respiratory and photosynthetic electron transfer chains. These highly reactive molecules can react with many cell components and damage DNA, proteins, and lipids. Thus, their concentration has to be strictly controlled. For this purpose, aerobic organisms are equipped with nonenzymatic (ascorbate, glutathione, tocopherol, and carotenoid) or enzymatic (catalase, ascorbate peroxidase, superoxide dismutase, glutathione peroxidase, and peroxiredoxin) antioxidant systems to remove ROS from the cells. To control their concentrations, ROS and RNS have to be sensed. It has been established in many organisms that ROS, and especially hydrogen peroxide, are signaling molecules that diffuse across membranes and induce specific signal transduction pathways. Furthermore, ROS can also be produced on purpose by cells in response to several stimuli to function as second messengers inside the cell. Finally, ROS and RNS can control enzyme activities by triggering several post-translational modifications such as disulfide bond formation, thiol oxidation to sulfenic/sulfinic/sulfonic acid, glutathionylation, nitrosylation, or carbonylation.Thiol/selenol peroxidases have emerged, during recent years, as important scavengers of ROS/RNS but they ...

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“…The enzyme not only detoxifies organic hydroperoxides but is also involved in the degradation of low concentrations of intracellular H 2 O 2 (29). The physiological functions and biochemical properties of other members of the Prx family, such as Tpx (thiol peroxidase), bactoferritin comigratory protein (BCP), 1-Cys Prx, and 2-Cys Prx, are less clear partly due to their limited distribution in only a few bacterial species (4,13,26,34). Nonetheless, they have been shown to be capable of metabolizing organic hydroperoxide.…”

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confidence: 99%

ohrR and ohr Are the Primary Sensor/Regulator and Protective Genes against Organic Hydroperoxide Stress in Agrobacterium tumefaciens

et al. 2006

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The genes involved in organic hydroperoxide protection in Agrobacterium tumefaciens were functionally evaluated. Gene inactivation studies and functional analyses have identified ohr, encoding a thiol peroxidase, as the gene primarily responsible for organic hydroperoxide protection in A. tumefaciens. An ohr mutant was sensitive to organic hydroperoxide killing and had a reduced capacity to metabolize organic hydroperoxides. ohr is located next to, and is divergently transcribed from, ohrR, encoding a sensor and transcription regulator of organic hydroperoxide stress. Transcription of both ohr and ohrR was induced by exposure to organic hydroperoxides but not by exposure to other oxidants. This induction required functional ohrR. The results of gel mobility shift and DNase I footprinting assays with purified OhrR, combined with in vivo promoter deletion analyses, confirmed that OhrR regulated both ohrR and ohr by binding to a single OhrR binding box that overlapped the ohrR and ohr promoters. ohrR and ohr are both required for the establishment of a novel cumene hydroperoxide-induced adaptive response. Inactivation or overexpression of other Prx family genes (prx1, prx2, prx3, bcp1, and bcp2) did not affect either the resistance to, or the ability to degrade, organic hydroperoxide. Taken together, the results of biochemical, gene regulation and physiological studies support the role of ohrR and ohr as the primary system in sensing and protecting A. tumefaciens from organic hydroperoxide stress.

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Vibrio cholerae Thiol Peroxidase-Glutaredoxin Fusion Is a 2-Cys TSA/AhpC Subfamily Acting as a Lipid Hydroperoxide Reductase

Cited by 24 publications

References 32 publications

Roles of Alkyl Hydroperoxide Reductase Subunit C (AhpC) in Viable but Nonculturable Vibrio parahaemolyticus

Roles of Alkyl Hydroperoxide Reductase Subunit C (AhpC) in Viable but Nonculturable Vibrio parahaemolyticus

The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

ohrR and ohr Are the Primary Sensor/Regulator and Protective Genes against Organic Hydroperoxide Stress in Agrobacterium tumefaciens

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